Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cullin-4

Gene

cul4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Required, indirectly, for activation of ribonucleotide reductase through the degradation of the protein spd1, thereby supplying deoxyribonucleotides for DNA replication and repair. Also has a role as a scaffold for assembling ubiquitin ligases. Component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.3 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • cellular protein localization Source: PomBase
  • chromatin silencing at centromere Source: PomBase
  • chromatin silencing at silent mating-type cassette Source: PomBase
  • chromatin silencing at telomere Source: PomBase
  • chromatin silencing by small RNA Source: PomBase
  • heterochromatin assembly Source: PomBase
  • negative regulation of transcription by RNA polymerase II Source: PomBase
  • positive regulation of meiotic cell cycle Source: PomBase
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of histone H3-K9 methylation Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • transcription-coupled nucleotide-excision repair Source: PomBase
  • ubiquitin-dependent protein catabolic process Source: InterPro

Keywordsi

Molecular functionChromatin regulator
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-SPO-110314 Recognition of DNA damage by PCNA-containing replication complex
R-SPO-5696395 Formation of Incision Complex in GG-NER
R-SPO-5696400 Dual Incision in GG-NER
R-SPO-6781823 Formation of TC-NER Pre-Incision Complex
R-SPO-6782135 Dual incision in TC-NER
R-SPO-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-SPO-8951664 Neddylation
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-4
Short name:
Cul-4
Gene namesi
Name:cul4
Synonyms:pcu4
ORF Names:SPAC3A11.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC3A11.08
PomBaseiSPAC3A11.08

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi680K → R: Increase in H3-K4 methylation within heterochromatin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001198101 – 734Cullin-4Add BLAST734

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki680Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity

Post-translational modificationi

Neddylated; enhancing the ubiquitin-ligase activity.By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO14122
PaxDbiO14122
PRIDEiO14122

PTM databases

iPTMnetiO14122

Interactioni

Subunit structurei

Component of the rik1-associated E3 ubiquitin ligase complex composed of at least clr4, cul4, pip1, raf1 and raf2.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi279548, 15 interactors
IntActiO14122, 7 interactors
STRINGi4896.SPAC3A11.08.1

Structurei

3D structure databases

ProteinModelPortaliO14122
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiO14122
KOiK10609
OMAiDFRHKLF
OrthoDBiEOG092C1L4K
PhylomeDBiO14122

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016157 Cullin_CS
IPR016158 Cullin_homology
IPR036317 Cullin_homology_sf
IPR001373 Cullin_N
IPR019559 Cullin_neddylation_domain
IPR016159 Cullin_repeat-like_dom_sf
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00888 Cullin, 1 hit
PF10557 Cullin_Nedd8, 1 hit
SMARTiView protein in SMART
SM00182 CULLIN, 1 hit
SM00884 Cullin_Nedd8, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF74788 SSF74788, 1 hit
SSF75632 SSF75632, 1 hit
PROSITEiView protein in PROSITE
PS01256 CULLIN_1, 1 hit
PS50069 CULLIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

O14122-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPEAKRIVV KGFDPRKSRQ RQETYYVTMI DRLNMALQVV MAGLGLKTGY
60 70 80 90 100
QELYSGVENL TRADQASRCF NILQHHMSSG IQLLKDSAES FIQLEGTETD
110 120 130 140 150
TNACTVVVGC WNKWLERVEI VQNIFYYMDK TFLSHHPDYP TIEELSLSLF
160 170 180 190 200
REKLMAVKNI QIPFLNSLLQ SFENLHSSKS TDHAYLQDAM LMLHRTEMYS
210 220 230 240 250
SVFVPMYLVM LSRFYDTESS QKIQELPLEE YLEYAMSSLE REDAYVEKFD
260 270 280 290 300
IVRDKKSIRE TVQRCLITSH LDTLTKGISQ FIEKRDAHSC KLLYALLQFN
310 320 330 340 350
HETEYLIQPW SDCLVDVGFK LVNDESKDDT LVQELLSFHK FLQVVVDESF
360 370 380 390 400
LHDETLSYAM RKAFETFING AKGSQREAPA RLIAKYIDYL LRVGEQASGG
410 420 430 440 450
KPLKEVFSEI LDLFRYIASK DIFEAYYKLD IAKRLLLNKS ASAQNELMLL
460 470 480 490 500
DMLKKTCGSQ FTHSLEGMFR DVNISKEFTS SFRHSKAAHN LHRDLYVNVL
510 520 530 540 550
SQAYWPSYPE SHIRLPDDMQ QDLDCFEKFY LSKQVGKKIS WYASLGHCIV
560 570 580 590 600
KARFPLGNKE LSISLFQACV LLQFNNCLGG EGISYQDLKK STELSDIDLT
610 620 630 640 650
RTLQSLSCAR IRPLVMVPKS KKPSPDTMFY VNEKFTDKLY RVKINQIYLK
660 670 680 690 700
EERQENSDVQ EQVVRDRQFE LQASIVRVMK QKEKMKHDDL VQYVINNVKD
710 720 730
RGIPLVSDVK TAIEKLLEKE YLEREDNDIY TYVT
Length:734
Mass (Da):85,330
Last modified:January 1, 1998 - v1
Checksum:iE90FFFE06D071C3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA Translation: CAB16383.1
AB017029 Genomic DNA Translation: BAA32520.1
AB027893 Genomic DNA Translation: BAA87197.1
PIRiT43408
RefSeqiNP_594195.1, NM_001019619.2

Genome annotation databases

EnsemblFungiiSPAC3A11.08.1; SPAC3A11.08.1:pep; SPAC3A11.08
GeneIDi2543116
KEGGispo:SPAC3A11.08

Similar proteinsi

Entry informationi

Entry nameiCUL4_SCHPO
AccessioniPrimary (citable) accession number: O14122
Secondary accession number(s): Q9USB6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: April 25, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health